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Diffusional increase and decrease in half-maximal-activity substrate concentrations with two-substrate enzymic

J M Engasser, P Hisland

    The Biochemical Journal
    |July 1, 1978
    PubMed
    Summary
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    Diffusional effects in enzyme reactions are influenced by substrate affinity. High-affinity substrates experience increased diffusion limitations, while low-affinity substrates show decreased limitations.

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Biophysical chemistry

    Background:

    • Enzymic reactions involve multiple substrates.
    • Substrate diffusion can impact reaction rates.
    • Enzyme-substrate affinity is a key factor in reaction dynamics.

    Purpose of the Study:

    • To investigate the influence of diffusional effects on two-substrate enzymic reactions.
    • To determine how relative substrate affinities affect these diffusional limitations.

    Main Methods:

    • Theoretical modeling of enzyme kinetics.
    • Analysis of diffusional effects based on substrate affinity parameters.

    Main Results:

    • Diffusional limitations are primarily dependent on the relative affinities of the enzyme for its two substrates.

    Related Experiment Videos

  • When substrate affinities differ significantly, diffusion limitations alter the half-maximal-activity concentration (K_m,app) for both substrates.
  • Specifically, diffusional limitations increase the K_m,app for the high-affinity substrate and decrease it for the low-affinity substrate.

    • Conclusions:

    • The relative substrate affinities critically modulate the impact of diffusion on two-substrate enzyme kinetics.
    • Understanding these effects is crucial for accurately interpreting enzyme reaction mechanisms and kinetics in biological systems.